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Homocitrate synthase

From Wikipedia, the free encyclopedia
homocitrate synthase
Homocitrate synthase homodimer, Schizosaccharomyces pombe
Identifiers
EC no.2.3.3.14
CAS no.9075-60-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a homocitrate synthase (EC 2.3.3.14) is an enzyme that catalyzes the chemical reaction

 
 
H2O
 
Reversible left-right reaction arrow with minor forward substrate(s) from top left and minor reverse product(s) to bottom left
H2O
 
 
 

The three substrates of this enzyme are α-ketoglutaric acid, acetyl-CoA, and water. Its products are (-)-homoisocitric acid and coenzyme A.[1][2][3][4]

This enzyme belongs to the family of transferases, specifically those acyltransferases that convert acyl groups into alkyl groups on transfer. The systematic name of this enzyme class is acetyl-CoA:2-oxoglutarate C-acetyltransferase (thioester-hydrolysing, carboxymethyl forming). Other names in common use include 2-hydroxybutane-1,2,4-tricarboxylate 2-oxoglutarate-lyase, (CoA-acetylating), acetyl-coenzyme A:2-ketoglutarate C-acetyl transferase, and homocitrate synthetase. This enzyme participates in lysine biosynthesis and pyruvate metabolism.

References

[edit]
  1. ^ Enzyme 2.3.3.14 at KEGG Pathway Database.
  2. ^ Strassman M, Ceci LN (1964). "Enzymatic formation of homocitric acid, an intermediate in lysine biosynthesis". Biochem. Biophys. Res. Commun. 14 (3): 262–7. Bibcode:1964BBRC...14..262S. doi:10.1016/0006-291X(64)90446-2. PMID 5836514.
  3. ^ H; Miyazaki, J; Kobashi, N; Nishiyama, M; Hoshino, T; Yamane, H (2002). "Characterization of bacterial homocitrate synthase involved in lysine biosynthesis". FEBS Lett. 522 (1–3): 35–40. Bibcode:2002FEBSL.522...35W. doi:10.1016/S0014-5793(02)02877-6. PMID 12095615.
  4. ^ Andi B, West AH, Cook PF (2004). "Kinetic mechanism of histidine-tagged homocitrate synthase from Saccharomyces cerevisiae". Biochemistry. 43 (37): 11790–5. doi:10.1021/bi048766p. PMID 15362863.